3RYH

GMPCPP-Tubulin: RB3 Stathmin-like domain complex

3RYH の概要

• エントリーDOI: 10.2210/pdb3ryh/pdb
• 関連するPDBエントリー: 3RYC 3RYF 3RYI
• 分子名称: Tubulin alpha chain, Tubulin beta chain, Stathmin-4, ... (8 entities in total)
• 機能のキーワード: alpha-tubulin, beta-tubulin, gmpcpp, gtpase, microtubule, stathmin s-tubulin, subtilisin, tubulin, cell cycle
• 由来する生物種: Rattus norvegicus (rat); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 220197.11

構造登録者

Nawrotek, A.,Knossow, M.,Gigant, B. (登録日: 2011-05-11, 公開日: 2011-10-05, 最終更新日: 2023-09-13)

主引用文献

Nawrotek, A.,Knossow, M.,Gigant, B.
The Determinants That Govern Microtubule Assembly from the Atomic Structure of GTP-Tubulin.
J.Mol.Biol., 412:35-42, 2011

PubMed Abstract: Tubulin alternates between a soluble curved structure and a microtubule straight conformation. GTP binding to αβ-tubulin is required for microtubule assembly, but whether this triggers conversion into a straighter structure is still debated. This is due, at least in part, to the lack of structural data for GTP-tubulin before assembly. Here, we report atomic-resolution crystal structures of soluble tubulin in the GDP and GTP nucleotide states in a complex with a stathmin-like domain. The structures differ locally in the neighborhood of the nucleotide. A loop movement in GTP-bound tubulin favors its recruitment to the ends of growing microtubules and facilitates its curved-to-straight transition, but this conversion has not proceeded yet. The data therefore argue for the conformational change toward the straight structure occurring as microtubule-specific contacts are established. They also suggest a model for the way the tubulin structure is modified in relation to microtubule assembly.

PubMed: 21787788
DOI: 10.1016/j.jmb.2011.07.029

実験手法

X-RAY DIFFRACTION (2.8 Å)